Towards an understanding of the structural and functional properties of MscL, a mechanosensitive channel in bacteria

Paul Blount, Sergei I. Sukharev, Paul C. Moe, Scott K. Nagle, Ching Kung

Research output: Contribution to journalReview articlepeer-review

50 Scopus citations

Abstract

Whether it be to sense a touch, arterial pressure, or an osmotic gradient across a cell membrane, essentially all living organisms require the capability of detecting mechanical force. Electrophysiological evidence has suggested that mechanosensitive ion channels play a major role in many systems where mechanical force is detected. But, despite their biological importance, determination of the most basic structural and functional features of mechanosensitive channels has only recently become possible. A gene called mscL, which was isolated from Escherichia coli, was the first gene shown to encode a mechanosensitive channel activity. This channel directly responds to tension in the membrane; no other proteins are required. MscL appears to be a homohexamer of a 136 amino acid polypeptide that is highly a helical, contains two transmembrane domains, and has both the amino and carboxyl termini in the cytoplasm. The study of the MscL protein remains, to date, one of the most viable options for understanding the structural and functional characteristics of a mechanosensitive channel.

Original languageEnglish (US)
Pages (from-to)1-8
Number of pages8
JournalBiology of the Cell
Volume87
Issue number1-2
DOIs
StatePublished - 1996

Keywords

  • Escherichia coli
  • Mechanosensation
  • Mechanosensitive channel
  • Patch-clamp
  • Stretch activated channel

ASJC Scopus subject areas

  • Cell Biology

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